NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1999329963|ref|XP_039795152|]
View 

DNA mismatch repair protein MSH6-like isoform X1 [Panicum virgatum]

Protein Classification

MutS family DNA mismatch repair protein( domain architecture ID 15333065)

MutS family DNA mismatch repair protein similar to human DNA mismatch repair proteins Msh2 (MutS protein homolog 2) and Msh3 (MutS protein homolog 3), components of the MutS beta heterodimer, which binds to DNA with mismatched base pairs and initiates repair

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
MutS super family cl33816
DNA mismatch repair ATPase MutS [Replication, recombination and repair];
362-1312 3.02e-168

DNA mismatch repair ATPase MutS [Replication, recombination and repair];


The actual alignment was detected with superfamily member COG0249:

Pssm-ID: 440019 [Multi-domain]  Cd Length: 861  Bit Score: 524.24  E-value: 3.02e-168
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  362 RQWWEFKSQHMDKVLFFKMGKFYELFEMDAHVGAKDLDL------QYMKGEQPHCGFPEKNLSVNLEKLAKKGYRVLVVE 435
Cdd:COG0249     12 QQYLEIKAQYPDALLFFRMGDFYELFFEDAEKASRLLDItltkrgKGAGEPIPMAGVPYHAAEGYLAKLVKAGYKVAICE 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  436 QTETPEQfelrrkAMGIkdkvcfdsvvsVKviscveatskcdipkfsaklfgmlysRKVVRreicaMVTKGTLTEgEHLL 515
Cdd:COG0249     92 QVEDPAE------AKGL-----------VK--------------------------REVVR-----VVTPGTLTE-DALL 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  516 ANPDPSYLLSVTEslqqssNKSQYtciiGVCIVDVSTSKFIVGQFqDDPERhgLCSILSEMRPVEIIKPGKMLSPET-EK 594
Cdd:COG0249    123 DAKRNNYLAAVAR------DKGRY----GLAWLDISTGEFLVTEL-DGEEA--LLDELARLAPAEILVPEDLPDPEElLE 189
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  595 ALKNntREPLINELlPSTEFwDAEKTINEIKKYYSSAdkqnnvdnvqdSLESLpnllseliGAGDKTYALSALGGSLFYL 674
Cdd:COG0249    190 LLRE--RGAAVTRL-PDWAF-DPDAARRRLLEQFGVA-----------SLDGF--------GLEDLPAAIAAAGALLAYL 246
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  675 RQTLldekivpCAEFEPLacSGI-INNIRKHMILDSAALENLELLENIRtGGVSGTLYAQLNHCVTGFGKRLLKRWIARP 753
Cdd:COG0249    247 EETQ-------KGALPHL--RRLrRYEEDDYLILDAATRRNLELTETLR-GGRKGSLLSVLDRTVTAMGSRLLRRWLLRP 316
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  754 LYDCRAILQRQRAIATFKgvgNNYA--AQFRKDLCRLPDMERLLARLFSRcdgnkRsssivlyedASKRLLqqftAALRg 831
Cdd:COG0249    317 LRDRAAIEARLDAVEELL---EDPLlrEELRELLKGVYDLERLLSRIALG-----R---------ANPRDL----AALR- 374
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  832 ceQMFHACSLISTLICTEDSvdSQLNDLLspgKGLPNVSYILDRFRDAFdwseAD------RNGRIIpLQGCDPEYDATC 905
Cdd:COG0249    375 --DSLAALPELKELLAELDS--PLLAELA---EALDPLEDLAELLERAI----VDepplliRDGGVI-REGYDAELDELR 442
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  906 NAIQEIESSLKEYLKEQRKLLRCAS--VTYVNV-GkdmYLIEVPESLGGSVPGNYQLQSTKKGSYRYWTPELKELISELS 982
Cdd:COG0249    443 ELSENGKEWLAELEARERERTGIKSlkVGYNKVfG---YYIEVTKANADKVPDDYIRKQTLKNAERYITPELKELEDKIL 519
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  983 KAEA-----EKEsklkgILQNLIQLFVEHHSEWRQLVSVVAELDVLISLAIAS---NYfegpsCCPTIkesngsDDTPTF 1054
Cdd:COG0249    520 SAEEralalEYE-----LFEELREEVAAHIERLQALARALAELDVLASLAEVAvenNY-----VRPEL------DDSPGI 583
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1055 HARNLGHPILRSdSLGKGSFVPNDVKIGGpgNSSFIVLTGPNMGGKSTLLRQVCLTIILAQIGADVPAENLELSLVDRIF 1134
Cdd:COG0249    584 EIEGGRHPVVEQ-ALPGEPFVPNDCDLDP--DRRILLITGPNMAGKSTYMRQVALIVLLAQIGSFVPAESARIGIVDRIF 660
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1135 VRMGARDHIMAGQSTFLVELMETASVLSSATKNSFVALDELGRGTSTSDGQAIAASVLDYLVHQVQCLGLFSTHYHRL-A 1213
Cdd:COG0249    661 TRVGASDDLARGQSTFMVEMTETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAVAEYLHDKIRARTLFATHYHELtE 740
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1214 VEHKDTKVSLCHMAC-EVGkgegglEEVTFLYRLTAGACPKSYGVNVARLAGIPASVLLRANEKSIDFEANYGKrccvTK 1292
Cdd:COG0249    741 LAEKLPGVKNYHVAVkEWG------GDIVFLHKVVPGPADRSYGIHVAKLAGLPASVIERAREILAELEKGEAA----AA 810
                          970       980
                   ....*....|....*....|....*.
gi 1999329963 1293 DKHASSQ------HEDEFSAIRDVLR 1312
Cdd:COG0249    811 GKAAPDQlslfaaADPEPSPVLEELK 836
Tudor_Agenet_AtEML-like cd20404
Tudor-like Agenet domain found in Arabidopsis thaliana proteins EMSY-LIKE 1-4 (AtEML1-4) and ...
104-153 3.34e-23

Tudor-like Agenet domain found in Arabidopsis thaliana proteins EMSY-LIKE 1-4 (AtEML1-4) and similar proteins; This family includes Arabidopsis thaliana proteins EMSY-LIKE 1-4 (AtEML1-4), histone-lysine N-methyltransferase trithorax-like proteins ATX1-2 (AtATX1-2), histone-lysine N-methyltransferase ASHH3, DNA mismatch repair protein MSH6, and similar proteins. EMSY-like proteins contain an EMSY N-terminal domain, a central Tudor-like Agenet domain, and a C-terminal coiled-coil motif. AtEML1, AtEML2, and likely AtEML4, contribute to RPP7-mediated immunity. Besides this, AtEML1 and AtEML2 participate in a second EDM2-dependent function and affect floral transition. ATX-like proteins are plant counterparts of the Drosophila melanogaster trithorax (TRX) and mammalian mixed-lineage leukemia (MLL1) proteins. ATX1, also called protein SET domain group 27, or trithorax-homolog protein 1 (TRX-homolog protein 1), is a methyltransferase that trimethylates histone H3 at lysine 4 (H3K4me3). It also acts as a histone modifier and as a positive effector of gene expression. ATX1regulates transcription from diverse classes of genes implicated in biotic and abiotic stress responses. It is involved in dehydration stress signaling in both abscisic acid (ABA)-dependent and ABA-independent pathways. ATX2, also called protein SET domain group 30, or trithorax-homolog protein 2 (TRX-homolog protein 2), is involved in dimethylating histone H3 at lysine 4 (H3K4me2). Both ATX1 and ATX2 are multi-domain proteins that consist of an N-terminal Tudor-like Agenet domain, a PWWP domain, FYRN- and FYRC (DAST, domain associated with SET in trithorax) domains, a canonical plant homeodomain (PHD) domain, a non-canonical extended PHD (ePHD) domain, and a C-terminal SET domain. ASHR3, also called protein SET DOMAIN GROUP 7, functions as a histone-lysine N-methyltransferase (EC 2.1.1.43). It contains a SET domain and a Tudor-like Agenet domain. AtMSH6, also called MutS protein homolog 6, is a component of the post-replicative DNA mismatch repair system (MMR). It forms a heterodimer with MutS alpha (MSH2-MSH6 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. AtMSH6 contains a Tudor-like Agenet domain and a MutS domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


:

Pssm-ID: 410475 [Multi-domain]  Cd Length: 51  Bit Score: 93.50  E-value: 3.34e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1999329963  104 GRRLRVYWPLDDAWYEGRVDAYDAGSRKHRVKYDDGEEEQVDLGKERFEW 153
Cdd:cd20404      2 GRRVRVYWPEDGTWYEGVVVDYDPSTGKHRVEYDDGDEEEVDLWRELVEW 51
 
Name Accession Description Interval E-value
MutS COG0249
DNA mismatch repair ATPase MutS [Replication, recombination and repair];
362-1312 3.02e-168

DNA mismatch repair ATPase MutS [Replication, recombination and repair];


Pssm-ID: 440019 [Multi-domain]  Cd Length: 861  Bit Score: 524.24  E-value: 3.02e-168
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  362 RQWWEFKSQHMDKVLFFKMGKFYELFEMDAHVGAKDLDL------QYMKGEQPHCGFPEKNLSVNLEKLAKKGYRVLVVE 435
Cdd:COG0249     12 QQYLEIKAQYPDALLFFRMGDFYELFFEDAEKASRLLDItltkrgKGAGEPIPMAGVPYHAAEGYLAKLVKAGYKVAICE 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  436 QTETPEQfelrrkAMGIkdkvcfdsvvsVKviscveatskcdipkfsaklfgmlysRKVVRreicaMVTKGTLTEgEHLL 515
Cdd:COG0249     92 QVEDPAE------AKGL-----------VK--------------------------REVVR-----VVTPGTLTE-DALL 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  516 ANPDPSYLLSVTEslqqssNKSQYtciiGVCIVDVSTSKFIVGQFqDDPERhgLCSILSEMRPVEIIKPGKMLSPET-EK 594
Cdd:COG0249    123 DAKRNNYLAAVAR------DKGRY----GLAWLDISTGEFLVTEL-DGEEA--LLDELARLAPAEILVPEDLPDPEElLE 189
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  595 ALKNntREPLINELlPSTEFwDAEKTINEIKKYYSSAdkqnnvdnvqdSLESLpnllseliGAGDKTYALSALGGSLFYL 674
Cdd:COG0249    190 LLRE--RGAAVTRL-PDWAF-DPDAARRRLLEQFGVA-----------SLDGF--------GLEDLPAAIAAAGALLAYL 246
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  675 RQTLldekivpCAEFEPLacSGI-INNIRKHMILDSAALENLELLENIRtGGVSGTLYAQLNHCVTGFGKRLLKRWIARP 753
Cdd:COG0249    247 EETQ-------KGALPHL--RRLrRYEEDDYLILDAATRRNLELTETLR-GGRKGSLLSVLDRTVTAMGSRLLRRWLLRP 316
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  754 LYDCRAILQRQRAIATFKgvgNNYA--AQFRKDLCRLPDMERLLARLFSRcdgnkRsssivlyedASKRLLqqftAALRg 831
Cdd:COG0249    317 LRDRAAIEARLDAVEELL---EDPLlrEELRELLKGVYDLERLLSRIALG-----R---------ANPRDL----AALR- 374
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  832 ceQMFHACSLISTLICTEDSvdSQLNDLLspgKGLPNVSYILDRFRDAFdwseAD------RNGRIIpLQGCDPEYDATC 905
Cdd:COG0249    375 --DSLAALPELKELLAELDS--PLLAELA---EALDPLEDLAELLERAI----VDepplliRDGGVI-REGYDAELDELR 442
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  906 NAIQEIESSLKEYLKEQRKLLRCAS--VTYVNV-GkdmYLIEVPESLGGSVPGNYQLQSTKKGSYRYWTPELKELISELS 982
Cdd:COG0249    443 ELSENGKEWLAELEARERERTGIKSlkVGYNKVfG---YYIEVTKANADKVPDDYIRKQTLKNAERYITPELKELEDKIL 519
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  983 KAEA-----EKEsklkgILQNLIQLFVEHHSEWRQLVSVVAELDVLISLAIAS---NYfegpsCCPTIkesngsDDTPTF 1054
Cdd:COG0249    520 SAEEralalEYE-----LFEELREEVAAHIERLQALARALAELDVLASLAEVAvenNY-----VRPEL------DDSPGI 583
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1055 HARNLGHPILRSdSLGKGSFVPNDVKIGGpgNSSFIVLTGPNMGGKSTLLRQVCLTIILAQIGADVPAENLELSLVDRIF 1134
Cdd:COG0249    584 EIEGGRHPVVEQ-ALPGEPFVPNDCDLDP--DRRILLITGPNMAGKSTYMRQVALIVLLAQIGSFVPAESARIGIVDRIF 660
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1135 VRMGARDHIMAGQSTFLVELMETASVLSSATKNSFVALDELGRGTSTSDGQAIAASVLDYLVHQVQCLGLFSTHYHRL-A 1213
Cdd:COG0249    661 TRVGASDDLARGQSTFMVEMTETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAVAEYLHDKIRARTLFATHYHELtE 740
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1214 VEHKDTKVSLCHMAC-EVGkgegglEEVTFLYRLTAGACPKSYGVNVARLAGIPASVLLRANEKSIDFEANYGKrccvTK 1292
Cdd:COG0249    741 LAEKLPGVKNYHVAVkEWG------GDIVFLHKVVPGPADRSYGIHVAKLAGLPASVIERAREILAELEKGEAA----AA 810
                          970       980
                   ....*....|....*....|....*.
gi 1999329963 1293 DKHASSQ------HEDEFSAIRDVLR 1312
Cdd:COG0249    811 GKAAPDQlslfaaADPEPSPVLEELK 836
PRK05399 PRK05399
DNA mismatch repair protein MutS; Provisional
354-1312 3.85e-163

DNA mismatch repair protein MutS; Provisional


Pssm-ID: 235444 [Multi-domain]  Cd Length: 854  Bit Score: 510.41  E-value: 3.85e-163
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  354 LKSLTGGQRQWWEFKSQHMDKVLFFKMGKFYELFEMDAHVGAKDLDL-----QYMKGEQ-PHCGFPEKNLSVNLEKLAKK 427
Cdd:PRK05399     5 MSKLTPMMQQYLEIKAQYPDALLFFRMGDFYELFFEDAKKASRLLDItltkrGKSAGEPiPMAGVPYHAAEGYLAKLVKK 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  428 GYRVLVVEQTETPEQfelrrkAMGIkdkvcfdsvvsVKviscveatskcdipkfsaklfgmlysRKVVRreicaMVTKGT 507
Cdd:PRK05399    85 GYKVAICEQVEDPAT------AKGP-----------VK--------------------------REVVR-----IVTPGT 116
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  508 LTEgEHLLANPDPSYLLSVTESlqqssnKSQYtciiGVCIVDVSTSKFIVGQFqdDPERhgLCSILSEMRPVEIIkpgkm 587
Cdd:PRK05399   117 VTD-EALLDEKQNNYLAAIAQD------GGGY----GLAYLDLSTGEFRVTEL--DEEE--LLAELARLNPAEIL----- 176
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  588 LSPETEKALKNNTREPLIneLLPSTEFwDAEKTINEIKKYYssadkqnnvdNVQdSLESLPNLLSEligagdktyALSAL 667
Cdd:PRK05399   177 VPEDFSEDELLLLRRGLR--RRPPWEF-DLDTAEKRLLEQF----------GVA-SLDGFGVDLPL---------AIRAA 233
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  668 GGSLFYLRQTLLDE-----KIVpcaefeplacsgiINNIRKHMILDSAALENLELLENIRtGGVSGTLYAQLNHCVTGFG 742
Cdd:PRK05399   234 GALLQYLKETQKRSlphlrSPK-------------RYEESDYLILDAATRRNLELTENLR-GGRKNSLLSVLDRTVTAMG 299
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  743 KRLLKRWIARPLYDCRAILQRQRAIATFKGvgnnyAAQFRKDLCRL----PDMERLLARLFSRcdgnkrsssivlyeDAS 818
Cdd:PRK05399   300 GRLLRRWLHRPLRDREAIEARLDAVEELLE-----DPLLREDLRELlkgvYDLERLLSRIALG--------------RAN 360
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  819 KRLLqqftAALRgceQMFHACSLISTLICTEDSvdSQLNDLLSPGKGLPNVSYILDRfrdafdwSEAD------RNGRII 892
Cdd:PRK05399   361 PRDL----AALR---DSLEALPELKELLAELDS--PLLAELAEQLDPLEELADLLER-------AIVEepplliRDGGVI 424
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  893 pLQGCDPEYDATCNAIQEIESSLKEYLKEQRKLLRCAS--VTYVNV-GkdmYLIEVPESLGGSVPGNYQLQSTKKGSYRY 969
Cdd:PRK05399   425 -ADGYDAELDELRALSDNGKDWLAELEARERERTGISSlkVGYNKVfG---YYIEVTKANLDKVPEDYIRRQTLKNAERY 500
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  970 WTPELKELISELSKAEA-----EKEsklkgILQNLIQLFVEHHSEWRQLVSVVAELDVLISLAIAS---NYfegpsCCPT 1041
Cdd:PRK05399   501 ITPELKELEDKILSAEEkalalEYE-----LFEELREEVAEHIERLQKLAKALAELDVLASLAEVAeenNY-----VRPE 570
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1042 IkesngsDDTPTFHARNLGHPILRSdSLGKGSFVPNDVKIGGpgNSSFIVLTGPNMGGKSTLLRQVCLTIILAQIGADVP 1121
Cdd:PRK05399   571 F------TDDPGIDIEEGRHPVVEQ-VLGGEPFVPNDCDLDE--ERRLLLITGPNMAGKSTYMRQVALIVLLAQIGSFVP 641
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1122 AENLELSLVDRIFVRMGARDHIMAGQSTFLVELMETASVLSSATKNSFVALDELGRGTSTSDGQAIAASVLDYLVHQVQC 1201
Cdd:PRK05399   642 AESARIGIVDRIFTRIGASDDLASGRSTFMVEMTETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAVAEYLHDKIGA 721
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1202 LGLFSTHYHRL-AVEHKDTKVSLCHM-ACEVGkgegglEEVTFLYRLTAGACPKSYGVNVARLAGIPASVLLRANEKSID 1279
Cdd:PRK05399   722 KTLFATHYHELtELEEKLPGVKNVHVaVKEHG------GDIVFLHKVVPGAADKSYGIHVAKLAGLPASVIKRAREILAQ 795
                          970       980       990
                   ....*....|....*....|....*....|....*..
gi 1999329963 1280 FEANYGKRccvTKDKHASSQH----EDEFSAIRDVLR 1312
Cdd:PRK05399   796 LESASEKA---KAASAEEDQLslfaEPEESPLLEALK 829
mutS1 TIGR01070
DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair]
357-1287 1.24e-126

DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273427 [Multi-domain]  Cd Length: 840  Bit Score: 412.63  E-value: 1.24e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  357 LTGGQRQWWEFKSQHMDKVLFFKMGKFYELFEMDAHVGAKDLDLQYMKGEQ------PHCGFPEKNLSVNLEKLAKKGYR 430
Cdd:TIGR01070    1 LTPMMQQYLKLKAEHPDALLFFRMGDFYELFYEDAKKAAQLLDISLTSRGQsadepiPMAGIPYHAVEAYLEKLVKQGES 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  431 VLVVEQTETPEQfelrrkamgikdkvcfdsvvsvkviscveatskcdipkfsaklfgmlySRKVVRREICAMVTKGTLTE 510
Cdd:TIGR01070   81 VAICEQIEDPKT------------------------------------------------AKGPVEREVVQLITPGTVSD 112
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  511 gEHLLANPDPSYLLSVTeslqQSSNKsqytciIGVCIVDVSTSKFIVGQFQDdpeRHGLCSILSEMRPVEIIKPGkmlsp 590
Cdd:TIGR01070  113 -EALLPERQDNLLAAIA----QESNG------FGLATLDLTTGEFKVTELAD---KETLYAELQRLNPAEVLLAE----- 173
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  591 etekalknntreplinELLPSTEFWDAEKTINEIKKYYssadkqnnvdNVQDSLESLPNLlsELIGAGDKTYALSALggs 670
Cdd:TIGR01070  174 ----------------DLSEMEAIELREFRKDTAVMSL----------EAQFGTEDLGGL--GLRNAPLGLTAAGCL--- 222
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  671 LFYLRQTLLDE--KIVPCAEFEPLACsgiinnirkhMILDSAALENLELLENIRtGGVSGTLYAQLNHCVTGFGKRLLKR 748
Cdd:TIGR01070  223 LQYAKRTQRTAlpHLQPVRLYELQDF----------MQLDAATRRNLELTENLR-GGKQNTLFSVLDETKTAMGSRLLKR 291
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  749 WIARPLYDCRAILQRQRAIATFKGVGNnYAAQFRKDLCRLPDMERLLARL-FSRcdgnkrsssivlyedASKRLLQQFTA 827
Cdd:TIGR01070  292 WLHRPLRDREVLEARQDTVEVLLRHFF-LREGLRPLLKEVGDLERLAARVaLGN---------------ARPRDLARLRT 355
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  828 ALRGCEQmfhacslISTLICTEDSVDSQlndllSPGKGLPNVSYILDRFRDAF--DWSEADRNGRIIPlQGCDPEYDATC 905
Cdd:TIGR01070  356 SLEQLPE-------LRALLEELEGPTLQ-----ALAAQIDDFSELLELLEAALieNPPLVVRDGGLIR-EGYDEELDELR 422
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  906 NAIQEIESSLKEYLKEQRKL--LRCASVTYVNVgkDMYLIEVPESLGGSVPGNYQLQSTKKGSYRYWTPELKELISELSK 983
Cdd:TIGR01070  423 AASREGTDYLARLEARERERtgIPTLKVGYNAV--FGYYIEVTRGQLHLVPAHYRRRQTLKNAERYITPELKEKEDKVLE 500
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  984 AEAEKESKLKGILQNLIQLFVEHHSEWRQLVSVVAELDVLISLA-IASNY-FEGPSCCptikesngsdDTPTFHARNLGH 1061
Cdd:TIGR01070  501 AEGKILALEKELFEELRELLKKYLEALQEAARALAELDVLANLAeVAETLhYTRPRFG----------DDPQLRIREGRH 570
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1062 PILrsDSLGKGSFVPNDVKIGGpgNSSFIVLTGPNMGGKSTLLRQVCLTIILAQIGADVPAENLELSLVDRIFVRMGARD 1141
Cdd:TIGR01070  571 PVV--EQVLRTPFVPNDLEMAH--NRRMLLITGPNMGGKSTYMRQTALIALLAQIGSFVPAESAELPLFDRIFTRIGASD 646
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1142 HIMAGQSTFLVELMETASVLSSATKNSFVALDELGRGTSTSDGQAIAASVLDYLVHQVQCLGLFSTHYHRL-AVEHKDTK 1220
Cdd:TIGR01070  647 DLASGRSTFMVEMTEAANILHNATENSLVLFDEIGRGTSTYDGLALAWAIAEYLHEHIRAKTLFATHYFELtALEESLPG 726
                          890       900       910       920       930       940
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1999329963 1221 VSLCHMACEVGKGeggleEVTFLYRLTAGACPKSYGVNVARLAGIPASVLLRANEKSIDFEANYGKR 1287
Cdd:TIGR01070  727 LKNVHVAALEHNG-----TIVFLHQVLPGPASKSYGLAVAALAGLPKEVIARARQILTQLEARSTES 788
ABC_MSH6_euk cd03286
ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA ...
1056-1273 8.50e-96

ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.


Pssm-ID: 213253 [Multi-domain]  Cd Length: 218  Bit Score: 306.28  E-value: 8.50e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1056 ARNLGHPILRSDSlgKGSFVPNDVKIGGpGNSSFIVLTGPNMGGKSTLLRQVCLTIILAQIGADVPAENLELSLVDRIFV 1135
Cdd:cd03286      2 FEELRHPCLNAST--ASSFVPNDVDLGA-TSPRILVLTGPNMGGKSTLLRTVCLAVIMAQMGMDVPAKSMRLSLVDRIFT 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1136 RMGARDHIMAGQSTFLVELMETASVLSSATKNSFVALDELGRGTSTSDGQAIAASVLDYLVHQVQCLGLFSTHYHRLAVE 1215
Cdd:cd03286     79 RIGARDDIMKGESTFMVELSETANILRHATPDSLVILDELGRGTSTHDGYAIAHAVLEYLVKKVKCLTLFSTHYHSLCDE 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1216 -HKDTKVSLCHMACEV-GKGEGGLEEVTFLYRLTAGACPKSYGVNVARLAGIPASVLLRA 1273
Cdd:cd03286    159 fHEHGGVRLGHMACAVkNESDPTIRDITFLYKLVAGICPKSYGLYVALMAGIPDGVVERA 218
MUTSac smart00534
ATPase domain of DNA mismatch repair MUTS family;
1089-1277 2.72e-86

ATPase domain of DNA mismatch repair MUTS family;


Pssm-ID: 197777 [Multi-domain]  Cd Length: 185  Bit Score: 278.67  E-value: 2.72e-86
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  1089 FIVLTGPNMGGKSTLLRQVCLTIILAQIGADVPAENLELSLVDRIFVRMGARDHIMAGQSTFLVELMETASVLSSATKNS 1168
Cdd:smart00534    1 VVIITGPNMGGKSTYLRQVALIVIMAQIGSFVPAESAELPVFDRIFTRIGASDSLAQGLSTFMVEMKETANILKNATKNS 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  1169 FVALDELGRGTSTSDGQAIAASVLDYLVHQVQCLGLFSTHYHRLAV-EHKDTKVSLCHMACEVGKgegglEEVTFLYRLT 1247
Cdd:smart00534   81 LVLLDELGRGTSTYDGLAIAAAILEYLLEKIGARTLFATHYHELTKlADNHPGVRNLHMSALEET-----ENITFLYKLK 155
                           170       180       190
                    ....*....|....*....|....*....|
gi 1999329963  1248 AGACPKSYGVNVARLAGIPASVLLRANEKS 1277
Cdd:smart00534  156 PGVAGKSYGIEVAKLAGLPKEVIERAKRIL 185
MutS_V pfam00488
MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ...
1090-1281 2.65e-80

MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair proteins) and is found associated with pfam01624, pfam05188, pfam05192 and pfam05190. The mutS family of proteins is named after the Salmonella typhimurium MutS protein involved in mismatch repair; other members of the family included the eukaryotic MSH 1,2,3, 4,5 and 6 proteins. These have various roles in DNA repair and recombination. Human MSH has been implicated in non-polyposis colorectal carcinoma (HNPCC) and is a mismatch binding protein. The aligned region corresponds with domain V of Thermus aquaticus MutS as characterized in, which contains a Walker A motif, and is structurally similar to the ATPase domain of ABC transporters.


Pssm-ID: 425714 [Multi-domain]  Cd Length: 188  Bit Score: 261.74  E-value: 2.65e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1090 IVLTGPNMGGKSTLLRQVCLTIILAQIGADVPAENLELSLVDRIFVRMGARDHIMAGQSTFLVELMETASVLSSATKNSF 1169
Cdd:pfam00488    1 LIITGPNMGGKSTYLRQVALIVLMAQIGSFVPAESAEIGIVDRIFTRIGASDDLAKGRSTFMVEMLETANILHNATDKSL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1170 VALDELGRGTSTSDGQAIAASVLDYLVHQVQCLGLFSTHYHRL-AVEHKDTKVSLCHMACEvgkgEGGlEEVTFLYRLTA 1248
Cdd:pfam00488   81 VILDELGRGTSTYDGLAIAWAVAEHLAEKIKARTLFATHYHELtKLAEKLPAVKNLHMAAV----EDD-DDIVFLYKVQP 155
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1999329963 1249 GACPKSYGVNVARLAGIPASVLLRANEKSIDFE 1281
Cdd:pfam00488  156 GAADKSYGIHVAELAGLPESVVERAREILAELE 188
Tudor_Agenet_AtEML-like cd20404
Tudor-like Agenet domain found in Arabidopsis thaliana proteins EMSY-LIKE 1-4 (AtEML1-4) and ...
104-153 3.34e-23

Tudor-like Agenet domain found in Arabidopsis thaliana proteins EMSY-LIKE 1-4 (AtEML1-4) and similar proteins; This family includes Arabidopsis thaliana proteins EMSY-LIKE 1-4 (AtEML1-4), histone-lysine N-methyltransferase trithorax-like proteins ATX1-2 (AtATX1-2), histone-lysine N-methyltransferase ASHH3, DNA mismatch repair protein MSH6, and similar proteins. EMSY-like proteins contain an EMSY N-terminal domain, a central Tudor-like Agenet domain, and a C-terminal coiled-coil motif. AtEML1, AtEML2, and likely AtEML4, contribute to RPP7-mediated immunity. Besides this, AtEML1 and AtEML2 participate in a second EDM2-dependent function and affect floral transition. ATX-like proteins are plant counterparts of the Drosophila melanogaster trithorax (TRX) and mammalian mixed-lineage leukemia (MLL1) proteins. ATX1, also called protein SET domain group 27, or trithorax-homolog protein 1 (TRX-homolog protein 1), is a methyltransferase that trimethylates histone H3 at lysine 4 (H3K4me3). It also acts as a histone modifier and as a positive effector of gene expression. ATX1regulates transcription from diverse classes of genes implicated in biotic and abiotic stress responses. It is involved in dehydration stress signaling in both abscisic acid (ABA)-dependent and ABA-independent pathways. ATX2, also called protein SET domain group 30, or trithorax-homolog protein 2 (TRX-homolog protein 2), is involved in dimethylating histone H3 at lysine 4 (H3K4me2). Both ATX1 and ATX2 are multi-domain proteins that consist of an N-terminal Tudor-like Agenet domain, a PWWP domain, FYRN- and FYRC (DAST, domain associated with SET in trithorax) domains, a canonical plant homeodomain (PHD) domain, a non-canonical extended PHD (ePHD) domain, and a C-terminal SET domain. ASHR3, also called protein SET DOMAIN GROUP 7, functions as a histone-lysine N-methyltransferase (EC 2.1.1.43). It contains a SET domain and a Tudor-like Agenet domain. AtMSH6, also called MutS protein homolog 6, is a component of the post-replicative DNA mismatch repair system (MMR). It forms a heterodimer with MutS alpha (MSH2-MSH6 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. AtMSH6 contains a Tudor-like Agenet domain and a MutS domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410475 [Multi-domain]  Cd Length: 51  Bit Score: 93.50  E-value: 3.34e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1999329963  104 GRRLRVYWPLDDAWYEGRVDAYDAGSRKHRVKYDDGEEEQVDLGKERFEW 153
Cdd:cd20404      2 GRRVRVYWPEDGTWYEGVVVDYDPSTGKHRVEYDDGDEEEVDLWRELVEW 51
 
Name Accession Description Interval E-value
MutS COG0249
DNA mismatch repair ATPase MutS [Replication, recombination and repair];
362-1312 3.02e-168

DNA mismatch repair ATPase MutS [Replication, recombination and repair];


Pssm-ID: 440019 [Multi-domain]  Cd Length: 861  Bit Score: 524.24  E-value: 3.02e-168
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  362 RQWWEFKSQHMDKVLFFKMGKFYELFEMDAHVGAKDLDL------QYMKGEQPHCGFPEKNLSVNLEKLAKKGYRVLVVE 435
Cdd:COG0249     12 QQYLEIKAQYPDALLFFRMGDFYELFFEDAEKASRLLDItltkrgKGAGEPIPMAGVPYHAAEGYLAKLVKAGYKVAICE 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  436 QTETPEQfelrrkAMGIkdkvcfdsvvsVKviscveatskcdipkfsaklfgmlysRKVVRreicaMVTKGTLTEgEHLL 515
Cdd:COG0249     92 QVEDPAE------AKGL-----------VK--------------------------REVVR-----VVTPGTLTE-DALL 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  516 ANPDPSYLLSVTEslqqssNKSQYtciiGVCIVDVSTSKFIVGQFqDDPERhgLCSILSEMRPVEIIKPGKMLSPET-EK 594
Cdd:COG0249    123 DAKRNNYLAAVAR------DKGRY----GLAWLDISTGEFLVTEL-DGEEA--LLDELARLAPAEILVPEDLPDPEElLE 189
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  595 ALKNntREPLINELlPSTEFwDAEKTINEIKKYYSSAdkqnnvdnvqdSLESLpnllseliGAGDKTYALSALGGSLFYL 674
Cdd:COG0249    190 LLRE--RGAAVTRL-PDWAF-DPDAARRRLLEQFGVA-----------SLDGF--------GLEDLPAAIAAAGALLAYL 246
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  675 RQTLldekivpCAEFEPLacSGI-INNIRKHMILDSAALENLELLENIRtGGVSGTLYAQLNHCVTGFGKRLLKRWIARP 753
Cdd:COG0249    247 EETQ-------KGALPHL--RRLrRYEEDDYLILDAATRRNLELTETLR-GGRKGSLLSVLDRTVTAMGSRLLRRWLLRP 316
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  754 LYDCRAILQRQRAIATFKgvgNNYA--AQFRKDLCRLPDMERLLARLFSRcdgnkRsssivlyedASKRLLqqftAALRg 831
Cdd:COG0249    317 LRDRAAIEARLDAVEELL---EDPLlrEELRELLKGVYDLERLLSRIALG-----R---------ANPRDL----AALR- 374
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  832 ceQMFHACSLISTLICTEDSvdSQLNDLLspgKGLPNVSYILDRFRDAFdwseAD------RNGRIIpLQGCDPEYDATC 905
Cdd:COG0249    375 --DSLAALPELKELLAELDS--PLLAELA---EALDPLEDLAELLERAI----VDepplliRDGGVI-REGYDAELDELR 442
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  906 NAIQEIESSLKEYLKEQRKLLRCAS--VTYVNV-GkdmYLIEVPESLGGSVPGNYQLQSTKKGSYRYWTPELKELISELS 982
Cdd:COG0249    443 ELSENGKEWLAELEARERERTGIKSlkVGYNKVfG---YYIEVTKANADKVPDDYIRKQTLKNAERYITPELKELEDKIL 519
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  983 KAEA-----EKEsklkgILQNLIQLFVEHHSEWRQLVSVVAELDVLISLAIAS---NYfegpsCCPTIkesngsDDTPTF 1054
Cdd:COG0249    520 SAEEralalEYE-----LFEELREEVAAHIERLQALARALAELDVLASLAEVAvenNY-----VRPEL------DDSPGI 583
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1055 HARNLGHPILRSdSLGKGSFVPNDVKIGGpgNSSFIVLTGPNMGGKSTLLRQVCLTIILAQIGADVPAENLELSLVDRIF 1134
Cdd:COG0249    584 EIEGGRHPVVEQ-ALPGEPFVPNDCDLDP--DRRILLITGPNMAGKSTYMRQVALIVLLAQIGSFVPAESARIGIVDRIF 660
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1135 VRMGARDHIMAGQSTFLVELMETASVLSSATKNSFVALDELGRGTSTSDGQAIAASVLDYLVHQVQCLGLFSTHYHRL-A 1213
Cdd:COG0249    661 TRVGASDDLARGQSTFMVEMTETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAVAEYLHDKIRARTLFATHYHELtE 740
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1214 VEHKDTKVSLCHMAC-EVGkgegglEEVTFLYRLTAGACPKSYGVNVARLAGIPASVLLRANEKSIDFEANYGKrccvTK 1292
Cdd:COG0249    741 LAEKLPGVKNYHVAVkEWG------GDIVFLHKVVPGPADRSYGIHVAKLAGLPASVIERAREILAELEKGEAA----AA 810
                          970       980
                   ....*....|....*....|....*.
gi 1999329963 1293 DKHASSQ------HEDEFSAIRDVLR 1312
Cdd:COG0249    811 GKAAPDQlslfaaADPEPSPVLEELK 836
PRK05399 PRK05399
DNA mismatch repair protein MutS; Provisional
354-1312 3.85e-163

DNA mismatch repair protein MutS; Provisional


Pssm-ID: 235444 [Multi-domain]  Cd Length: 854  Bit Score: 510.41  E-value: 3.85e-163
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  354 LKSLTGGQRQWWEFKSQHMDKVLFFKMGKFYELFEMDAHVGAKDLDL-----QYMKGEQ-PHCGFPEKNLSVNLEKLAKK 427
Cdd:PRK05399     5 MSKLTPMMQQYLEIKAQYPDALLFFRMGDFYELFFEDAKKASRLLDItltkrGKSAGEPiPMAGVPYHAAEGYLAKLVKK 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  428 GYRVLVVEQTETPEQfelrrkAMGIkdkvcfdsvvsVKviscveatskcdipkfsaklfgmlysRKVVRreicaMVTKGT 507
Cdd:PRK05399    85 GYKVAICEQVEDPAT------AKGP-----------VK--------------------------REVVR-----IVTPGT 116
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  508 LTEgEHLLANPDPSYLLSVTESlqqssnKSQYtciiGVCIVDVSTSKFIVGQFqdDPERhgLCSILSEMRPVEIIkpgkm 587
Cdd:PRK05399   117 VTD-EALLDEKQNNYLAAIAQD------GGGY----GLAYLDLSTGEFRVTEL--DEEE--LLAELARLNPAEIL----- 176
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  588 LSPETEKALKNNTREPLIneLLPSTEFwDAEKTINEIKKYYssadkqnnvdNVQdSLESLPNLLSEligagdktyALSAL 667
Cdd:PRK05399   177 VPEDFSEDELLLLRRGLR--RRPPWEF-DLDTAEKRLLEQF----------GVA-SLDGFGVDLPL---------AIRAA 233
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  668 GGSLFYLRQTLLDE-----KIVpcaefeplacsgiINNIRKHMILDSAALENLELLENIRtGGVSGTLYAQLNHCVTGFG 742
Cdd:PRK05399   234 GALLQYLKETQKRSlphlrSPK-------------RYEESDYLILDAATRRNLELTENLR-GGRKNSLLSVLDRTVTAMG 299
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  743 KRLLKRWIARPLYDCRAILQRQRAIATFKGvgnnyAAQFRKDLCRL----PDMERLLARLFSRcdgnkrsssivlyeDAS 818
Cdd:PRK05399   300 GRLLRRWLHRPLRDREAIEARLDAVEELLE-----DPLLREDLRELlkgvYDLERLLSRIALG--------------RAN 360
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  819 KRLLqqftAALRgceQMFHACSLISTLICTEDSvdSQLNDLLSPGKGLPNVSYILDRfrdafdwSEAD------RNGRII 892
Cdd:PRK05399   361 PRDL----AALR---DSLEALPELKELLAELDS--PLLAELAEQLDPLEELADLLER-------AIVEepplliRDGGVI 424
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  893 pLQGCDPEYDATCNAIQEIESSLKEYLKEQRKLLRCAS--VTYVNV-GkdmYLIEVPESLGGSVPGNYQLQSTKKGSYRY 969
Cdd:PRK05399   425 -ADGYDAELDELRALSDNGKDWLAELEARERERTGISSlkVGYNKVfG---YYIEVTKANLDKVPEDYIRRQTLKNAERY 500
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  970 WTPELKELISELSKAEA-----EKEsklkgILQNLIQLFVEHHSEWRQLVSVVAELDVLISLAIAS---NYfegpsCCPT 1041
Cdd:PRK05399   501 ITPELKELEDKILSAEEkalalEYE-----LFEELREEVAEHIERLQKLAKALAELDVLASLAEVAeenNY-----VRPE 570
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1042 IkesngsDDTPTFHARNLGHPILRSdSLGKGSFVPNDVKIGGpgNSSFIVLTGPNMGGKSTLLRQVCLTIILAQIGADVP 1121
Cdd:PRK05399   571 F------TDDPGIDIEEGRHPVVEQ-VLGGEPFVPNDCDLDE--ERRLLLITGPNMAGKSTYMRQVALIVLLAQIGSFVP 641
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1122 AENLELSLVDRIFVRMGARDHIMAGQSTFLVELMETASVLSSATKNSFVALDELGRGTSTSDGQAIAASVLDYLVHQVQC 1201
Cdd:PRK05399   642 AESARIGIVDRIFTRIGASDDLASGRSTFMVEMTETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAVAEYLHDKIGA 721
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1202 LGLFSTHYHRL-AVEHKDTKVSLCHM-ACEVGkgegglEEVTFLYRLTAGACPKSYGVNVARLAGIPASVLLRANEKSID 1279
Cdd:PRK05399   722 KTLFATHYHELtELEEKLPGVKNVHVaVKEHG------GDIVFLHKVVPGAADKSYGIHVAKLAGLPASVIKRAREILAQ 795
                          970       980       990
                   ....*....|....*....|....*....|....*..
gi 1999329963 1280 FEANYGKRccvTKDKHASSQH----EDEFSAIRDVLR 1312
Cdd:PRK05399   796 LESASEKA---KAASAEEDQLslfaEPEESPLLEALK 829
mutS1 TIGR01070
DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair]
357-1287 1.24e-126

DNA mismatch repair protein MutS; [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273427 [Multi-domain]  Cd Length: 840  Bit Score: 412.63  E-value: 1.24e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  357 LTGGQRQWWEFKSQHMDKVLFFKMGKFYELFEMDAHVGAKDLDLQYMKGEQ------PHCGFPEKNLSVNLEKLAKKGYR 430
Cdd:TIGR01070    1 LTPMMQQYLKLKAEHPDALLFFRMGDFYELFYEDAKKAAQLLDISLTSRGQsadepiPMAGIPYHAVEAYLEKLVKQGES 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  431 VLVVEQTETPEQfelrrkamgikdkvcfdsvvsvkviscveatskcdipkfsaklfgmlySRKVVRREICAMVTKGTLTE 510
Cdd:TIGR01070   81 VAICEQIEDPKT------------------------------------------------AKGPVEREVVQLITPGTVSD 112
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  511 gEHLLANPDPSYLLSVTeslqQSSNKsqytciIGVCIVDVSTSKFIVGQFQDdpeRHGLCSILSEMRPVEIIKPGkmlsp 590
Cdd:TIGR01070  113 -EALLPERQDNLLAAIA----QESNG------FGLATLDLTTGEFKVTELAD---KETLYAELQRLNPAEVLLAE----- 173
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  591 etekalknntreplinELLPSTEFWDAEKTINEIKKYYssadkqnnvdNVQDSLESLPNLlsELIGAGDKTYALSALggs 670
Cdd:TIGR01070  174 ----------------DLSEMEAIELREFRKDTAVMSL----------EAQFGTEDLGGL--GLRNAPLGLTAAGCL--- 222
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  671 LFYLRQTLLDE--KIVPCAEFEPLACsgiinnirkhMILDSAALENLELLENIRtGGVSGTLYAQLNHCVTGFGKRLLKR 748
Cdd:TIGR01070  223 LQYAKRTQRTAlpHLQPVRLYELQDF----------MQLDAATRRNLELTENLR-GGKQNTLFSVLDETKTAMGSRLLKR 291
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  749 WIARPLYDCRAILQRQRAIATFKGVGNnYAAQFRKDLCRLPDMERLLARL-FSRcdgnkrsssivlyedASKRLLQQFTA 827
Cdd:TIGR01070  292 WLHRPLRDREVLEARQDTVEVLLRHFF-LREGLRPLLKEVGDLERLAARVaLGN---------------ARPRDLARLRT 355
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  828 ALRGCEQmfhacslISTLICTEDSVDSQlndllSPGKGLPNVSYILDRFRDAF--DWSEADRNGRIIPlQGCDPEYDATC 905
Cdd:TIGR01070  356 SLEQLPE-------LRALLEELEGPTLQ-----ALAAQIDDFSELLELLEAALieNPPLVVRDGGLIR-EGYDEELDELR 422
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  906 NAIQEIESSLKEYLKEQRKL--LRCASVTYVNVgkDMYLIEVPESLGGSVPGNYQLQSTKKGSYRYWTPELKELISELSK 983
Cdd:TIGR01070  423 AASREGTDYLARLEARERERtgIPTLKVGYNAV--FGYYIEVTRGQLHLVPAHYRRRQTLKNAERYITPELKEKEDKVLE 500
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  984 AEAEKESKLKGILQNLIQLFVEHHSEWRQLVSVVAELDVLISLA-IASNY-FEGPSCCptikesngsdDTPTFHARNLGH 1061
Cdd:TIGR01070  501 AEGKILALEKELFEELRELLKKYLEALQEAARALAELDVLANLAeVAETLhYTRPRFG----------DDPQLRIREGRH 570
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1062 PILrsDSLGKGSFVPNDVKIGGpgNSSFIVLTGPNMGGKSTLLRQVCLTIILAQIGADVPAENLELSLVDRIFVRMGARD 1141
Cdd:TIGR01070  571 PVV--EQVLRTPFVPNDLEMAH--NRRMLLITGPNMGGKSTYMRQTALIALLAQIGSFVPAESAELPLFDRIFTRIGASD 646
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1142 HIMAGQSTFLVELMETASVLSSATKNSFVALDELGRGTSTSDGQAIAASVLDYLVHQVQCLGLFSTHYHRL-AVEHKDTK 1220
Cdd:TIGR01070  647 DLASGRSTFMVEMTEAANILHNATENSLVLFDEIGRGTSTYDGLALAWAIAEYLHEHIRAKTLFATHYFELtALEESLPG 726
                          890       900       910       920       930       940
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1999329963 1221 VSLCHMACEVGKGeggleEVTFLYRLTAGACPKSYGVNVARLAGIPASVLLRANEKSIDFEANYGKR 1287
Cdd:TIGR01070  727 LKNVHVAALEHNG-----TIVFLHQVLPGPASKSYGLAVAALAGLPKEVIARARQILTQLEARSTES 788
ABC_MSH6_euk cd03286
ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA ...
1056-1273 8.50e-96

ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.


Pssm-ID: 213253 [Multi-domain]  Cd Length: 218  Bit Score: 306.28  E-value: 8.50e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1056 ARNLGHPILRSDSlgKGSFVPNDVKIGGpGNSSFIVLTGPNMGGKSTLLRQVCLTIILAQIGADVPAENLELSLVDRIFV 1135
Cdd:cd03286      2 FEELRHPCLNAST--ASSFVPNDVDLGA-TSPRILVLTGPNMGGKSTLLRTVCLAVIMAQMGMDVPAKSMRLSLVDRIFT 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1136 RMGARDHIMAGQSTFLVELMETASVLSSATKNSFVALDELGRGTSTSDGQAIAASVLDYLVHQVQCLGLFSTHYHRLAVE 1215
Cdd:cd03286     79 RIGARDDIMKGESTFMVELSETANILRHATPDSLVILDELGRGTSTHDGYAIAHAVLEYLVKKVKCLTLFSTHYHSLCDE 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1216 -HKDTKVSLCHMACEV-GKGEGGLEEVTFLYRLTAGACPKSYGVNVARLAGIPASVLLRA 1273
Cdd:cd03286    159 fHEHGGVRLGHMACAVkNESDPTIRDITFLYKLVAGICPKSYGLYVALMAGIPDGVVERA 218
MUTSac smart00534
ATPase domain of DNA mismatch repair MUTS family;
1089-1277 2.72e-86

ATPase domain of DNA mismatch repair MUTS family;


Pssm-ID: 197777 [Multi-domain]  Cd Length: 185  Bit Score: 278.67  E-value: 2.72e-86
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  1089 FIVLTGPNMGGKSTLLRQVCLTIILAQIGADVPAENLELSLVDRIFVRMGARDHIMAGQSTFLVELMETASVLSSATKNS 1168
Cdd:smart00534    1 VVIITGPNMGGKSTYLRQVALIVIMAQIGSFVPAESAELPVFDRIFTRIGASDSLAQGLSTFMVEMKETANILKNATKNS 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  1169 FVALDELGRGTSTSDGQAIAASVLDYLVHQVQCLGLFSTHYHRLAV-EHKDTKVSLCHMACEVGKgegglEEVTFLYRLT 1247
Cdd:smart00534   81 LVLLDELGRGTSTYDGLAIAAAILEYLLEKIGARTLFATHYHELTKlADNHPGVRNLHMSALEET-----ENITFLYKLK 155
                           170       180       190
                    ....*....|....*....|....*....|
gi 1999329963  1248 AGACPKSYGVNVARLAGIPASVLLRANEKS 1277
Cdd:smart00534  156 PGVAGKSYGIEVAKLAGLPKEVIERAKRIL 185
MutS_V pfam00488
MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair ...
1090-1281 2.65e-80

MutS domain V; This domain is found in proteins of the MutS family (DNA mismatch repair proteins) and is found associated with pfam01624, pfam05188, pfam05192 and pfam05190. The mutS family of proteins is named after the Salmonella typhimurium MutS protein involved in mismatch repair; other members of the family included the eukaryotic MSH 1,2,3, 4,5 and 6 proteins. These have various roles in DNA repair and recombination. Human MSH has been implicated in non-polyposis colorectal carcinoma (HNPCC) and is a mismatch binding protein. The aligned region corresponds with domain V of Thermus aquaticus MutS as characterized in, which contains a Walker A motif, and is structurally similar to the ATPase domain of ABC transporters.


Pssm-ID: 425714 [Multi-domain]  Cd Length: 188  Bit Score: 261.74  E-value: 2.65e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1090 IVLTGPNMGGKSTLLRQVCLTIILAQIGADVPAENLELSLVDRIFVRMGARDHIMAGQSTFLVELMETASVLSSATKNSF 1169
Cdd:pfam00488    1 LIITGPNMGGKSTYLRQVALIVLMAQIGSFVPAESAEIGIVDRIFTRIGASDDLAKGRSTFMVEMLETANILHNATDKSL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1170 VALDELGRGTSTSDGQAIAASVLDYLVHQVQCLGLFSTHYHRL-AVEHKDTKVSLCHMACEvgkgEGGlEEVTFLYRLTA 1248
Cdd:pfam00488   81 VILDELGRGTSTYDGLAIAWAVAEHLAEKIKARTLFATHYHELtKLAEKLPAVKNLHMAAV----EDD-DDIVFLYKVQP 155
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1999329963 1249 GACPKSYGVNVARLAGIPASVLLRANEKSIDFE 1281
Cdd:pfam00488  156 GAADKSYGIHVAELAGLPESVVERAREILAELE 188
ABC_MutS1 cd03284
ATP-binding cassette domain of MutS1 homolog; The MutS protein initiates DNA mismatch repair ...
1061-1275 3.14e-76

ATP-binding cassette domain of MutS1 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.


Pssm-ID: 213251 [Multi-domain]  Cd Length: 216  Bit Score: 251.42  E-value: 3.14e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1061 HPILRSdSLGKGSFVPNDVKIGGpgNSSFIVLTGPNMGGKSTLLRQVCLTIILAQIGADVPAENLELSLVDRIFVRMGAR 1140
Cdd:cd03284      7 HPVVEQ-VLDNEPFVPNDTELDP--ERQILLITGPNMAGKSTYLRQVALIALLAQIGSFVPASKAEIGVVDRIFTRIGAS 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1141 DHIMAGQSTFLVELMETASVLSSATKNSFVALDELGRGTSTSDGQAIAASVLDYLVHQVQCLGLFSTHYHRL-AVEHKDT 1219
Cdd:cd03284     84 DDLAGGRSTFMVEMVETANILNNATERSLVLLDEIGRGTSTYDGLSIAWAIVEYLHEKIGAKTLFATHYHELtELEGKLP 163
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1999329963 1220 KVSLCHMACEVGKGeggleEVTFLYRLTAGACPKSYGVNVARLAGIPASVLLRANE 1275
Cdd:cd03284    164 RVKNFHVAVKEKGG-----GVVFLHKIVEGAADKSYGIEVARLAGLPEEVIERARE 214
ABC_MutS_homologs cd03243
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ...
1057-1265 4.30e-70

ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.


Pssm-ID: 213210 [Multi-domain]  Cd Length: 202  Bit Score: 233.30  E-value: 4.30e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1057 RNLGHPILRSDSLGKgSFVPNDVKIGgpgNSSFIVLTGPNMGGKSTLLRQVCLTIILAQIGADVPAENLELSLVDRIFVR 1136
Cdd:cd03243      3 KGGRHPVLLALTKGE-TFVPNDINLG---SGRLLLITGPNMGGKSTYLRSIGLAVLLAQIGCFVPAESASIPLVDRIFTR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1137 MGARDHIMAGQSTFLVELMETASVLSSATKNSFVALDELGRGTSTSDGQAIAASVLDYLVhQVQCLGLFSTHYHRLAVEH 1216
Cdd:cd03243     79 IGAEDSISDGRSTFMAELLELKEILSLATPRSLVLIDELGRGTSTAEGLAIAYAVLEHLL-EKGCRTLFATHFHELADLP 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1217 KDTKVS-LCHMACEVGKGeggleEVTFLYRLTAGACPKSYGVNVARLAGI 1265
Cdd:cd03243    158 EQVPGVkNLHMEELITTG-----GLTFTYKLIDGICDPSYALQIAELAGL 202
ABC_MSH3_euk cd03287
ATP-binding cassette domain of eukaryotic MutS3 homolog; The MutS protein initiates DNA ...
1055-1273 8.81e-67

ATP-binding cassette domain of eukaryotic MutS3 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.


Pssm-ID: 213254 [Multi-domain]  Cd Length: 222  Bit Score: 224.67  E-value: 8.81e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1055 HARNLGHPILrsDSLGKGSFVPNDVKIGGPGNSSFIVlTGPNMGGKSTLLRQVCLTIILAQIGADVPAENLELSLVDRIF 1134
Cdd:cd03287      2 LIKEGRHPMI--ESLLDKSFVPNDIHLSAEGGYCQII-TGPNMGGKSSYIRQVALITIMAQIGSFVPASSATLSIFDSVL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1135 VRMGARDHIMAGQSTFLVELMETASVLSSATKNSFVALDELGRGTSTSDGQAIAASVLDYLVHQVQCLGLFSTHYHRLAV 1214
Cdd:cd03287     79 TRMGASDSIQHGMSTFMVELSETSHILSNCTSRSLVILDELGRGTSTHDGIAIAYATLHYLLEEKKCLVLFVTHYPSLGE 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1999329963 1215 --EHKDTKVSLCHM---ACEVGKGEGGLEEVTFLYRLTAGACPKSYGVNVARLAGIPASVLLRA 1273
Cdd:cd03287    159 ilRRFEGSIRNYHMsylESQKDFETSDSQSITFLYKLVRGLASRSFGLNVARLAGLPKSIISRA 222
ABC_MSH2_euk cd03285
ATP-binding cassette domain of eukaryotic MutS2 homolog; The MutS protein initiates DNA ...
1055-1281 9.24e-67

ATP-binding cassette domain of eukaryotic MutS2 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.


Pssm-ID: 213252 [Multi-domain]  Cd Length: 222  Bit Score: 224.56  E-value: 9.24e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1055 HARNLGHPILRSDSlgKGSFVPNDVKIGGpGNSSFIVLTGPNMGGKSTLLRQVCLTIILAQIGADVPAENLELSLVDRIF 1134
Cdd:cd03285      1 VLKEARHPCVEAQD--DVAFIPNDVTLTR-GKSRFLIITGPNMGGKSTYIRQIGVIVLMAQIGCFVPCDSADIPIVDCIL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1135 VRMGARDHIMAGQSTFLVELMETASVLSSATKNSFVALDELGRGTSTSDGQAIAASVLDYLVHQVQCLGLFSTHYHRL-A 1213
Cdd:cd03285     78 ARVGASDSQLKGVSTFMAEMLETAAILKSATENSLIIIDELGRGTSTYDGFGLAWAIAEYIATQIKCFCLFATHFHELtA 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1999329963 1214 VEHKDTKVSLCHMACEVGKGEGgleEVTFLYRLTAGACPKSYGVNVARLAGIPASVLLRANEKSIDFE 1281
Cdd:cd03285    158 LADEVPNVKNLHVTALTDDASR---TLTMLYKVEKGACDQSFGIHVAELANFPKEVIEMAKQKALELE 222
MUTSd smart00533
DNA-binding domain of DNA mismatch repair MUTS family;
727-1064 5.11e-60

DNA-binding domain of DNA mismatch repair MUTS family;


Pssm-ID: 214710 [Multi-domain]  Cd Length: 308  Bit Score: 208.69  E-value: 5.11e-60
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963   727 SGTLYAQLNHCVTGFGKRLLKRWIARPLYDCRAILQRQRAIATFkgVGNNYAAQ-FRKDLCRLPDMERLLARLFSRcdgn 805
Cdd:smart00533    1 KGSLFELLNHTKTPMGKRLLRRWLLQPLLDLKEINERLDAVEEL--VENPELRQkLRQLLKRIPDLERLLSRIERG---- 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963   806 krsssivlyedaskrllqqfTAALRGCEQMFHACSLISTLICTEDSVDSQLNDLLSpGKGLPNVSYILDRFRDAFDWSEA 885
Cdd:smart00533   75 --------------------RASPRDLLRLYDSLEGLKEIRQLLESLDGPLLGLLL-KVILEPLLELLELLLELLNDDDP 133
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963   886 DR-NGRIIPLQGCDPEYDATCNAIQEIESSLKEYLKEQRKLLRCASVTYVNVGKDMYLIEVPESLGGSVPGNYQLQSTKK 964
Cdd:smart00533  134 LEvNDGGLIKDGFDPELDELREKLEELEEELEELLKKEREELGIDSLKLGYNKVHGYYIEVTKSEAKKVPKDFIRRSSLK 213
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963   965 GSYRYWTPELKELISELSKAEAEKESKLKGILQNLIQLFVEHHSEWRQLVSVVAELDVLISLAIASnyFEGPSCCPTIke 1044
Cdd:smart00533  214 NTERFTTPELKELENELLEAKEEIERLEKEILRELLEKVLEYLEELRALAEALAELDVLLSLATLA--AEGNYVRPEF-- 289
                           330       340
                    ....*....|....*....|
gi 1999329963  1045 sngsDDTPTFHARNLGHPIL 1064
Cdd:smart00533  290 ----VDSGELEIKNGRHPVL 305
ABC_MSH5_euk cd03281
ATP-binding cassette domain of eukaryotic MutS5 homolog; The MutS protein initiates DNA ...
1057-1265 2.07e-51

ATP-binding cassette domain of eukaryotic MutS5 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.


Pssm-ID: 213248 [Multi-domain]  Cd Length: 213  Bit Score: 180.19  E-value: 2.07e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1057 RNLGHPILRsdsLGKGSFVPNDVKIGGpGNSSFIVLTGPNMGGKSTLLRQVCLTIILAQIGADVPAENLELSLVDRIFVR 1136
Cdd:cd03281      3 QGGRHPLLE---LFVDSFVPNDTEIGG-GGPSIMVITGPNSSGKSVYLKQVALIVFLAHIGSFVPADSATIGLVDKIFTR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1137 MGARDHIMAGQSTFLVELMETASVLSSATKNSFVALDELGRGTSTSDGQAIAASVLDYLvhqvQCLG------LFSTHYH 1210
Cdd:cd03281     79 MSSRESVSSGQSAFMIDLYQVSKALRLATRRSLVLIDEFGKGTDTEDGAGLLIATIEHL----LKRGpecprvIVSTHFH 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1999329963 1211 RLAVEH--KDT-KVSLCHMA-CEVGKGEGGLEEVTFLYRLTAGACPKSYGVNVARLAGI 1265
Cdd:cd03281    155 ELFNRSllPERlKIKFLTMEvLLNPTSTSPNEDITYLYRLVPGLADTSFAIHCAKLAGI 213
MutS_III pfam05192
MutS domain III; This domain is found in proteins of the MutS family (DNA mismatch repair ...
710-1027 5.01e-50

MutS domain III; This domain is found in proteins of the MutS family (DNA mismatch repair proteins) and is found associated with pfam00488, pfam05188, pfam01624 and pfam05190. The MutS family of proteins is named after the Salmonella typhimurium MutS protein involved in mismatch repair; other members of the family included the eukaryotic MSH 1,2,3, 4,5 and 6 proteins. These have various roles in DNA repair and recombination. Human MSH has been implicated in non-polyposis colorectal carcinoma (HNPCC) and is a mismatch binding protein. The aligned region corresponds with domain III, which is central to the structure of Thermus aquaticus MutS as characterized in.


Pssm-ID: 461579 [Multi-domain]  Cd Length: 291  Bit Score: 179.14  E-value: 5.01e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  710 AALENLELLENIRtGGVSGTLYAQLNHCVTGFGKRLLKRWIARPLYDCRAILQRQRAIATFKGVGNNYAAqFRKDLCRLP 789
Cdd:pfam05192    1 ATLRNLELTENLR-GGKEGSLLGLLDRTKTPMGSRLLRQWLLQPLTDLEEINERLDAVEELLENSELRED-LRELLRRLP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  790 DMERLLARLFSRcdgnkrsssivlyedasKRLLQQFTAALRGCEQMFHACSLISTLICTEDSVDSQLNDLLspgkglpnv 869
Cdd:pfam05192   79 DLERLLSRIALG-----------------KATPRDLLALLDSLEKLPLLKELLLEEKSALLGELASLAELL--------- 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  870 syildrfRDAFDWSEADRNGRI-IPLQGCDPEYDATCNAIQEIESSLKEYLKEQRKLLRCAS--VTYVNVGKDM-----Y 941
Cdd:pfam05192  133 -------EEAIDEEPPALLRDGgVIRDGYDEELDELRDLLLDGKRLLAKLEARERERTGIKSlkVLYNKVFGYYlllveY 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  942 LIEVPESLGGSVPGNYQLQSTKKGSYRYWTPELKELISELSKAEAEKESKLKGILQNLIQLFVEHHSEWRQLVSVVAELD 1021
Cdd:pfam05192  206 YIEVSKSQKDKVPDDYIRIQTTKNAERYITPELKELERKILQAEERLLALEKELFEELLEEVLEYIEVLRRAAEALAELD 285

                   ....*.
gi 1999329963 1022 VLISLA 1027
Cdd:pfam05192  286 VLLSLA 291
ABC_MSH4_euk cd03282
ATP-binding cassette domain of eukaryotic MutS4 homolog; The MutS protein initiates DNA ...
1061-1263 6.98e-38

ATP-binding cassette domain of eukaryotic MutS4 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.


Pssm-ID: 213249 [Multi-domain]  Cd Length: 204  Bit Score: 141.37  E-value: 6.98e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1061 HPILRSDslgKGSFVPNDVKIGgPGNSSFIVLTGPNMGGKSTLLRQVCLTIILAQIGADVPAENLELSLVDRIFVRMGAR 1140
Cdd:cd03282      7 HPILDRD---KKNFIPNDIYLT-RGSSRFHIITGPNMSGKSTYLKQIALLAIMAQIGCFVPAEYATLPIFNRLLSRLSND 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1141 DHIMAGQSTFLVELMETASVLSSATKNSFVALDELGRGTSTSDGQAIAASVLDYLVhQVQCLGLFSTHYHRLAV--EHKD 1218
Cdd:cd03282     83 DSMERNLSTFASEMSETAYILDYADGDSLVLIDELGRGTSSADGFAISLAILECLI-KKESTVFFATHFRDIAAilGNKS 161
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1999329963 1219 TKVSLcHM-ACEVGKGeggleEVTFLYRLTAGA-CPKSYGVNVARLA 1263
Cdd:cd03282    162 CVVHL-HMkAQSINSN-----GIEMAYKLVLGLyRIVDDGIRFVRVL 202
ABC_MutS-like cd03283
ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch ...
1056-1265 7.15e-35

ATP-binding cassette domain of MutS-like homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.


Pssm-ID: 213250 [Multi-domain]  Cd Length: 199  Bit Score: 132.42  E-value: 7.15e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1056 ARNLGHPILRSDSLgkgsfVPNDVKIGgpgNSSFIVLTGPNMGGKSTLLRQVCLTIILAQIGADVPAENLELSlVDRIFV 1135
Cdd:cd03283      2 AKNLGHPLIGREKR-----VANDIDME---KKNGILITGSNMSGKSTFLRTIGVNVILAQAGAPVCASSFELP-PVKIFT 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1136 RMGARDHIMAGQSTFLVELMETASVLSSATKN--SFVALDELGRGTSTSDGQAIAASVLDYLvHQVQCLGLFSTHYHRLA 1213
Cdd:cd03283     73 SIRVSDDLRDGISYFYAELRRLKEIVEKAKKGepVLFLLDEIFKGTNSRERQAASAAVLKFL-KNKNTIGIISTHDLELA 151
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1999329963 1214 -VEHKDTKVSLCHMACEVGKGeggleEVTFLYRLTAGACPKSYGVNVARLAGI 1265
Cdd:cd03283    152 dLLDLDSAVRNYHFREDIDDN-----KLIFDYKLKPGVSPTRNALRLMKKIGI 199
MutS_I pfam01624
MutS domain I; This domain is found in proteins of the MutS family (DNA mismatch repair ...
358-512 1.49e-34

MutS domain I; This domain is found in proteins of the MutS family (DNA mismatch repair proteins) and is found associated with pfam00488, pfam05188, pfam05192 and pfam05190. The MutS family of proteins is named after the Salmonella typhimurium MutS protein involved in mismatch repair; other members of the family included the eukaryotic MSH 1,2,3, 4,5 and 6 proteins. These have various roles in DNA repair and recombination. Human MSH has been implicated in non-polyposis colorectal carcinoma (HNPCC) and is a mismatch binding protein. The aligned region corresponds with globular domain I, which is involved in DNA binding, in Thermus aquaticus MutS as characterized in.


Pssm-ID: 426350 [Multi-domain]  Cd Length: 113  Bit Score: 128.09  E-value: 1.49e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  358 TGGQRQWWEFKSQHMDKVLFFKMGKFYELFEMDAHVGAKDLDLQYMKGEQ------PHCGFPEKNLSVNLEKLAKKGYRV 431
Cdd:pfam01624    1 TPMMRQYLELKSKYPDAVLFFRVGDFYELFGEDAEIAARELGITLTVRKGgsgkriPMAGVPEHAFERYARRLVNKGYKV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  432 LVVEQTETPEQfelrrkamgikdkvcfdsvvsvkviscveatskcdipkfsaklfgmlySRKVVRREICAMVTKGTLTEG 511
Cdd:pfam01624   81 AICEQTETPAE------------------------------------------------AKGVVKREVVRVVTPGTLTDD 112

                   .
gi 1999329963  512 E 512
Cdd:pfam01624  113 E 113
mutS2 TIGR01069
MutS2 family protein; Function of MutS2 is unknown. It should not be considered a DNA mismatch ...
894-1276 7.08e-32

MutS2 family protein; Function of MutS2 is unknown. It should not be considered a DNA mismatch repair protein. It is likely a DNA mismatch binding protein of unknown cellular function. [DNA metabolism, Other]


Pssm-ID: 130141 [Multi-domain]  Cd Length: 771  Bit Score: 134.56  E-value: 7.08e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  894 LQGCDPEYDATCNAI----QEIESSLKEYL--KEQRKLLRCASVTYVNvgkDMYLIEVPESLGGSVPGNYqLQSTKKGSY 967
Cdd:TIGR01069  141 KDGASEELDAIRESLkaleEEVVKRLHKIIrsKELAKYLSDTIVTIRN---GRYVLPLKSGFKGKIKGIV-HDTSSSGET 216
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  968 RYWTPE-LKELISELSKAEAEKESKLKGILQNLIQLFVEHHSEWRQLVSVVAELDVLISLAIASNYFEGPSCCPTikesn 1046
Cdd:TIGR01069  217 FYIEPQaIVKLNNKLAQLKNEEECEIEKILRTLSEKVQEYLLELKFLFKEFDFLDSLQARARYAKAVKGEFPMPS----- 291
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1047 gsdDTPTFHARNLGHPILRSDSLgkgsfVPNDVKIGGpgNSSFIVLTGPNMGGKSTLLRQVCLTIILAQIGADVPA-ENL 1125
Cdd:TIGR01069  292 ---FTGKIILENARHPLLKEPKV-----VPFTLNLKF--EKRVLAITGPNTGGKTVTLKTLGLLALMFQSGIPIPAnEHS 361
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1126 ELSLVDRIFVRMGARDHIMAGQSTFLVELMETASVLSSATKNSFVALDELGRGTSTSDGQAIAASVLDYLvHQVQCLGLF 1205
Cdd:TIGR01069  362 EIPYFEEIFADIGDEQSIEQNLSTFSGHMKNISAILSKTTENSLVLFDELGAGTDPDEGSALAISILEYL-LKQNAQVLI 440
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1999329963 1206 STHYHRL-AVEHKDTKVSLCHMacevgkgEGGLEEVTFLYRLTAGACPKSYGVNVARLAGIPASVLLRANEK 1276
Cdd:TIGR01069  441 TTHYKELkALMYNNEGVENASV-------LFDEETLSPTYKLLKGIPGESYAFEIAQRYGIPHFIIEQAKTF 505
ABC_MutS2 cd03280
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS ...
1057-1265 5.14e-28

ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.


Pssm-ID: 213247 [Multi-domain]  Cd Length: 200  Bit Score: 112.73  E-value: 5.14e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1057 RNLGHPILrsdSLGKGSFVPNDVKIGGpgNSSFIVLTGPNMGGKSTLLRQVCLTIILAQIGADVPA-ENLELSLVDRIFV 1135
Cdd:cd03280      3 REARHPLL---PLQGEKVVPLDIQLGE--NKRVLVITGPNAGGKTVTLKTLGLLTLMAQSGLPIPAaEGSSLPVFENIFA 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1136 RMGARDHIMAGQSTFLVELMETASVLSSATKNSFVALDELGRGTSTSDGQAIAASVLDYLvHQVQCLGLFSTHYHRL-AV 1214
Cdd:cd03280     78 DIGDEQSIEQSLSTFSSHMKNIARILQHADPDSLVLLDELGSGTDPVEGAALAIAILEEL-LERGALVIATTHYGELkAY 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1999329963 1215 EHKDTKVslchmacEVGKGEGGLEEVTFLYRLTAGACPKSYGVNVARLAGI 1265
Cdd:cd03280    157 AYKREGV-------ENASMEFDPETLKPTYRLLIGVPGRSNALEIARRLGL 200
MutS2 COG1193
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
973-1281 5.51e-28

dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];


Pssm-ID: 440806 [Multi-domain]  Cd Length: 784  Bit Score: 122.17  E-value: 5.51e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  973 ELKELISElSKAEAEKesklkgILQNLIQLFVEHHSEWRQLVSVVAELDVLISLAIASNYFEGpsCCPTIkesngsDDTP 1052
Cdd:COG1193    233 ELRELEAE-ERREIER------ILRELSALVREYAEELLENLEILAELDFIFAKARYALELKA--VKPEL------NDEG 297
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1053 TFHARNLGHPILrsdslGKGSFVPNDVKIGGPGNSsfIVLTGPNMGGKSTLLRQVCLTIILAQIGADVPA-ENLELSLVD 1131
Cdd:COG1193    298 YIKLKKARHPLL-----DLKKVVPIDIELGEDFRT--LVITGPNTGGKTVTLKTVGLLTLMAQSGLPIPAaEGSELPVFD 370
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1132 RIFVRMGarDHimagQ------STF------LVElmetasVLSSATKNSFVALDELGRGTSTSDGQAIAASVLDYLvHQV 1199
Cdd:COG1193    371 NIFADIG--DE----QsieqslSTFsshmtnIVE------ILEKADENSLVLLDELGAGTDPQEGAALAIAILEEL-LER 437
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1200 QCLGLFSTHYHRL---AVEHKDTKVSlchmACEvgkgeggLEEVTF--LYRLTAGACPKSYGVNVARLAGIPASVLLRA- 1273
Cdd:COG1193    438 GARVVATTHYSELkayAYNTEGVENA----SVE-------FDVETLspTYRLLIGVPGRSNAFEIARRLGLPEEIIERAr 506
                          330
                   ....*....|.
gi 1999329963 1274 ---NEKSIDFE 1281
Cdd:COG1193    507 ellGEESIDVE 517
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
1074-1213 1.36e-25

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 104.36  E-value: 1.36e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1074 FVPNDVkigGPGNSSFIVLTGPNMGGKSTLLRQVCLTIILA----------QIGADVPAENLELslvdrIFVRMGardhI 1143
Cdd:cd03227     11 FVPNDV---TFGEGSLTIITGPNGSGKSTILDAIGLALGGAqsatrrrsgvKAGCIVAAVSAEL-----IFTRLQ----L 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1999329963 1144 MAGQStflvELMETASVLSSATKN--SFVALDELGRGTSTSDGQAIAASVLDYLVHqvQCLGLFSTHYHRLA 1213
Cdd:cd03227     79 SGGEK----ELSALALILALASLKprPLYILDEIDRGLDPRDGQALAEAILEHLVK--GAQVIVITHLPELA 144
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
886-1213 1.89e-24

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 110.69  E-value: 1.89e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  886 DRNGRIipLQGCDPEYDATCNAIQEIESSLKEYL------KEQRKLLRCASVTYVNvgkDMYLIEVPESLGGSVPGNYQL 959
Cdd:PRK00409   140 DEEGEV--KDSASEKLRGIRRQLRRKKSRIREKLesiirsKSLQKYLQDTIITIRN---DRYVLPVKAEYKHAIKGIVHD 214
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  960 QSTKkGSYRYWTP----ELKELISEL-SKAEAEKESklkgILQNLIQLFVEHHSEWRQLVSVVAELDVLI-----SLAIA 1029
Cdd:PRK00409   215 QSSS-GATLYIEPqsvvELNNEIRELrNKEEQEIER----ILKELSAKVAKNLDFLKFLNKIFDELDFIFararyAKALK 289
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1030 SNyfegpscCPTIKESNgsddtpTFHARNLGHPILRSDSLgkgsfVPNDVKIGGPGNSsfIVLTGPNMGGKSTLLRQVCL 1109
Cdd:PRK00409   290 AT-------FPLFNDEG------KIDLRQARHPLLDGEKV-----VPKDISLGFDKTV--LVITGPNTGGKTVTLKTLGL 349
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1110 TIILAQIGADVPA-ENLELSLVDRIFVRMGARDHIMAGQSTFLVELMETASVLSSATKNSFVALDELGRGTSTSDGQAIA 1188
Cdd:PRK00409   350 AALMAKSGLPIPAnEPSEIPVFKEIFADIGDEQSIEQSLSTFSGHMTNIVRILEKADKNSLVLFDELGAGTDPDEGAALA 429
                          330       340
                   ....*....|....*....|....*
gi 1999329963 1189 ASVLDYLvHQVQCLGLFSTHYHRLA 1213
Cdd:PRK00409   430 ISILEYL-RKRGAKIIATTHYKELK 453
Tudor_Agenet_AtEML-like cd20404
Tudor-like Agenet domain found in Arabidopsis thaliana proteins EMSY-LIKE 1-4 (AtEML1-4) and ...
104-153 3.34e-23

Tudor-like Agenet domain found in Arabidopsis thaliana proteins EMSY-LIKE 1-4 (AtEML1-4) and similar proteins; This family includes Arabidopsis thaliana proteins EMSY-LIKE 1-4 (AtEML1-4), histone-lysine N-methyltransferase trithorax-like proteins ATX1-2 (AtATX1-2), histone-lysine N-methyltransferase ASHH3, DNA mismatch repair protein MSH6, and similar proteins. EMSY-like proteins contain an EMSY N-terminal domain, a central Tudor-like Agenet domain, and a C-terminal coiled-coil motif. AtEML1, AtEML2, and likely AtEML4, contribute to RPP7-mediated immunity. Besides this, AtEML1 and AtEML2 participate in a second EDM2-dependent function and affect floral transition. ATX-like proteins are plant counterparts of the Drosophila melanogaster trithorax (TRX) and mammalian mixed-lineage leukemia (MLL1) proteins. ATX1, also called protein SET domain group 27, or trithorax-homolog protein 1 (TRX-homolog protein 1), is a methyltransferase that trimethylates histone H3 at lysine 4 (H3K4me3). It also acts as a histone modifier and as a positive effector of gene expression. ATX1regulates transcription from diverse classes of genes implicated in biotic and abiotic stress responses. It is involved in dehydration stress signaling in both abscisic acid (ABA)-dependent and ABA-independent pathways. ATX2, also called protein SET domain group 30, or trithorax-homolog protein 2 (TRX-homolog protein 2), is involved in dimethylating histone H3 at lysine 4 (H3K4me2). Both ATX1 and ATX2 are multi-domain proteins that consist of an N-terminal Tudor-like Agenet domain, a PWWP domain, FYRN- and FYRC (DAST, domain associated with SET in trithorax) domains, a canonical plant homeodomain (PHD) domain, a non-canonical extended PHD (ePHD) domain, and a C-terminal SET domain. ASHR3, also called protein SET DOMAIN GROUP 7, functions as a histone-lysine N-methyltransferase (EC 2.1.1.43). It contains a SET domain and a Tudor-like Agenet domain. AtMSH6, also called MutS protein homolog 6, is a component of the post-replicative DNA mismatch repair system (MMR). It forms a heterodimer with MutS alpha (MSH2-MSH6 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. AtMSH6 contains a Tudor-like Agenet domain and a MutS domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410475 [Multi-domain]  Cd Length: 51  Bit Score: 93.50  E-value: 3.34e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1999329963  104 GRRLRVYWPLDDAWYEGRVDAYDAGSRKHRVKYDDGEEEQVDLGKERFEW 153
Cdd:cd20404      2 GRRVRVYWPEDGTWYEGVVVDYDPSTGKHRVEYDDGDEEEVDLWRELVEW 51
MutS_IV pfam05190
MutS family domain IV; This domain is found in proteins of the MutS family (DNA mismatch ...
896-987 1.40e-22

MutS family domain IV; This domain is found in proteins of the MutS family (DNA mismatch repair proteins) and is found associated with pfam01624, pfam05188, pfam05192 and pfam00488. The mutS family of proteins is named after the Salmonella typhimurium MutS protein involved in mismatch repair; other members of the family included the eukaryotic MSH 1,2,3, 4,5 and 6 proteins. These have various roles in DNA repair and recombination. Human MSH has been implicated in non-polyposis colorectal carcinoma (HNPCC) and is a mismatch binding protein. The aligned region corresponds in part with globular domain IV, which is involved in DNA binding, in Thermus aquaticus MutS as characterized in.


Pssm-ID: 398730 [Multi-domain]  Cd Length: 92  Bit Score: 93.06  E-value: 1.40e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  896 GCDPEYDATCNAIQEIESSLKEYLKEQRKLLRCASVTYVNVGKDMYLIEVPESLGGSVPGNYQLQSTKKGSYRYWTPELK 975
Cdd:pfam05190    1 GFDEELDELRDLLDELEKELEELEKKEREKLGIKSLKVGYNKVFGYYIEVTRSEAKKVPSNYIRRQTLKNGVRFTTPELK 80
                           90
                   ....*....|..
gi 1999329963  976 ELISELSKAEAE 987
Cdd:pfam05190   81 KLEDELLEAEEE 92
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
1055-1218 9.43e-09

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 55.71  E-value: 9.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1055 HARNLGHPILrsdslGKGSFVPNDVKIGgpgNSSFIVLTGPNMGGKSTLLRQVCLTIILAQIGADVPAENLELSLVDRIF 1134
Cdd:cd00267      1 EIENLSFRYG-----GRTALDNVSLTLK---AGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963 1135 VRMGARDHIMAGQStflvELMETASVLSSATKnsFVALDELGRGTSTSDGQAIAASVLDYLVHQVQclGLFSTHYHRLAV 1214
Cdd:cd00267     73 RRIGYVPQLSGGQR----QRVALARALLLNPD--LLLLDEPTSGLDPASRERLLELLRELAEEGRT--VIIVTHDPELAE 144

                   ....
gi 1999329963 1215 EHKD 1218
Cdd:cd00267    145 LAAD 148
MutS_II pfam05188
MutS domain II; This domain is found in proteins of the MutS family (DNA mismatch repair ...
521-681 6.36e-07

MutS domain II; This domain is found in proteins of the MutS family (DNA mismatch repair proteins) and is found associated with pfam00488, pfam01624, pfam05192 and pfam05190. The MutS family of proteins is named after the Salmonella typhimurium MutS protein involved in mismatch repair; other members of the family included the eukaryotic MSH 1,2,3, 4,5 and 6 proteins. These have various roles in DNA repair and recombination. Human MSH has been implicated in non-polyposis colorectal carcinoma (HNPCC) and is a mismatch binding protein. This domain corresponds to domain II in Thermus aquaticus MutS as characterized in, and has similarity resembles RNAse-H-like domains (see pfam00075).


Pssm-ID: 398728 [Multi-domain]  Cd Length: 133  Bit Score: 50.04  E-value: 6.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  521 SYLLSVTESLQQSsnksqytciIGVCIVDVSTSKFIVGQFQDDPErhgLCSILSEMRPVEIIKPGKMLSPETEKALKNNT 600
Cdd:pfam05188    1 NYLAAISRGDGNR---------YGLAFLDLSTGEFGVSEFEDFEE---LLAELSRLSPKELLLPESLSSSTVAESQKLLE 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1999329963  601 REPLINElLPSTEFwDAEKTINEIKKYYSSADkqnnvdnvqdsLESLpnllseliGAGDKTYALSALGGSLFYLRQTLLD 680
Cdd:pfam05188   69 LRLRVGR-RPTWLF-ELEHAYEDLNEDFGVED-----------LDGF--------GLEELPLALCAAGALISYLKETQKE 127

                   .
gi 1999329963  681 E 681
Cdd:pfam05188  128 N 128
Tudor_AtPTM-like cd20401
Tudor domain found in Arabidopsis thaliana DDT domain-containing protein PTM (AtPTM), Dirigent ...
104-146 8.11e-06

Tudor domain found in Arabidopsis thaliana DDT domain-containing protein PTM (AtPTM), Dirigent protein 17 (AtDIR17), and similar proteins; This family includes AtPTM and AtDIR17. AtPTM, also called DDT domain-containing protein 1, or PHD type transcription factor with transmembrane domains, is a membrane-bound transcription factor required for plastid-to-nucleus retrograde signaling. AtDIR17 imparts stereoselectivity on the phenoxy radical-coupling reaction, yielding optically active lignans from two molecules of coniferyl alcohol in the biosynthesis of lignans, flavonolignans, and alkaloids, and thus plays a central role in plant secondary metabolism. Members of this family contain one Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410472  Cd Length: 50  Bit Score: 44.09  E-value: 8.11e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1999329963  104 GRRLRVYwpLDDAWYEGRVDAYDAGSRKHRVKYDDGEEEQVDL 146
Cdd:cd20401      2 GRRVRKK--FDGEWFDGTVVSYDKKTGLYHVEYEDGDAEELTE 42
Tudor_SF cd04508
Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally ...
104-146 2.05e-05

Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally identified in the Tudor protein of Drosophila, that adopts a beta-barrel-like core structure containing four short beta-strands followed by an alpha-helical region. It binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions. Tudor domain-containing proteins may mediate protein-protein interactions required for various DNA-templated biological processes, such as RNA metabolism, as well as histone modification and the DNA damage response. Members of this superfamily contain one or more copies of the Tudor domain.


Pssm-ID: 410449 [Multi-domain]  Cd Length: 47  Bit Score: 42.96  E-value: 2.05e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1999329963  104 GRRLRVYWPLDDAWYEGRVDAYDaGSRKHRVKYDDGEEEQVDL 146
Cdd:cd04508      1 GDRVEAKWSDDGQWYPATVVAVN-DDGKYTVLFDDGNEEEVSE 42
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH